Junctional Adhesion Molecule 2 (JAM2) is a member of the immunoglobulin superfamily and is primarily localized at the tight junctions of both epithelial and endothelial cells . It plays a crucial role in cell adhesion, migration, and maintaining the integrity of cell junctions . The recombinant form of JAM2, often referred to as “Human Recombinant JAM2,” is utilized in various research and therapeutic applications.
JAM2 is a type I membrane protein that consists of an extracellular domain, a single transmembrane region, and a cytoplasmic tail . The extracellular domain is responsible for mediating homophilic (JAM2-JAM2) and heterophilic (JAM2-other proteins) interactions . These interactions are vital for the assembly and maintenance of tight junctions, which regulate paracellular permeability and maintain cell polarity .
JAM2 is involved in various cellular processes, including cell migration and adhesion . It acts as an adhesive ligand for interacting with a variety of immune cell types, such as leukocytes, and plays a role in lymphocyte homing to secondary lymphoid organs . JAM2’s interaction with other proteins, such as PDZ domain-containing scaffolding proteins, regulates cell-cell contact maturation and the generation of junctional complexes .
The expression of JAM2 is regulated by several factors, including hormones and cytokines . For instance, progesterone and leukemia inhibitory factor (LIF) have been shown to up-regulate JAM2 expression in the uterine luminal epithelium, which is crucial for blastocyst adhesion during early pregnancy . This regulation is mediated through the tyrosine phosphorylation of Stat3 .
Human Recombinant JAM2 is widely used in research to study its role in various physiological and pathological processes. It is also being explored for therapeutic applications, particularly in the context of inflammation, cancer, and reproductive health . The recombinant form allows for controlled studies and potential therapeutic interventions by mimicking the natural protein’s function.